A. K. Shukla

This study determines the cryo-EM structure of the Duffy antigen receptor bound to CCL7, revealing structural features that explain its unique functional properties and lack of G protein coupling.

This study presents cryo-EM structures and experimental data revealing how beta-arrestins interact with GPCRs, particularly those with phosphorylation in the third intracellular loop and intrinsically biased receptors.

This study presents cryo-EM structures of GPR109A-G-protein complexes with agonists and uses them to engineer biased agonists with reduced flushing effects.

This paper develops a pH-responsive A-motif DNA hydrogel that forms reversible structures and demonstrates its use in biosensing and cell surface detection.

This study presents structural insights into C3a-C3aR interactions and identifies a G-protein-biased agonist for the receptor.

This study presents cryo-EM structures of C5aR1 bound to C5a and a synthetic peptide, revealing conformational changes and G-protein coupling mechanisms.

This study uses single-molecule microscopy and simulations to show that beta-arrestin inserts into the lipid bilayer and interacts with receptors through lateral diffusion, challenging existing models of its function.

The paper identifies a phosphorylation motif in arrestin2-CCR5 complexes that is essential for stable interactions and functional activation of CCR5.

The paper presents structural snapshots of β-arrestins interacting with GPCRs, revealing a conserved 'lock-and-key' activation mechanism through specific phosphorylation patterns.

This study characterizes the biased agonism of CXCR4 and CXCR7, revealing differences in G-protein coupling, β-arrestin recruitment, and ERK1/2 activation.

This paper shows that a synthetic intrabody enhances β-arrestin endosomal trafficking and ERK1/2 activation in a GPCR mutant by promoting an active-like conformation.

The paper identifies two non-canonical GPCRs, D6R and C5aR2, that exclusively couple to β-arrestins and exhibit distinct GRK preferences and downstream signaling.

The paper presents a crystal structure of β-arrestin 2 bound to a phosphopeptide from ACKR3, revealing an alternative active conformation distinct from β-arrestin 1.

This study describes a method to purify native CCL7 and its isotopically labeled derivatives, enabling structural and functional studies of chemokine receptor interactions.

The paper identifies structural differences between β-arrestin isoforms using conformational sensors and domain-swapping, linking these differences to their distinct functional outcomes in GPCR signaling.

This study uses genetically encoded intrabody sensors to reveal structural and functional diversity in GPCR-β-arrestin complexes, showing distinct functional outcomes across different receptors.

This study investigates ligand bias at C5aR1 by comparing C5a and C5apep, showing differential activation of G proteins, βarr recruitment, endocytosis, and ERK1/2 phosphorylation.